-
Toshiko SHIOTSUBO
1983 Volume 47 Issue 11 Pages
2421-2425
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The gelatinization process of potato starch was isothermally investigated at 52.5-65.3°C. The degree of gelatinization was measured by an enzymic digestion method using glucoamylase. When the starch-water suspension was incubated at a definite temperature the gelatinization reached a limit at each temperature after 30-60 min incubation. So, it can be supposed that starch gelatinization reached an equilibrium state. It was found that gelatinization of potato starch occurred even at 52.5°C, a temperature which is lower than the so-called gelatinization temperature generally reported. Starch gelatinization was found to follow first order kinetics, and from the temperature dependence of the rate constants obtained, the activation energy was calculated to be 22±5 kcal/mol. The relationship between the degree of gelatinization of the starch whose gelatinization reached an equilibrium state at a definite temperature and the incubation temperature gave a transition curve expressed by the fraction of gelatinized potato starch granules as a function of temperature, and the half-transition temperature was found to be 59.1°C. From the transition curve. the van't Hoff enthalpy for gelatinization was determined to be+130±3kcal/mol.
View full abstract
-
Takashi HAMANO, Yukimasa MITSUHASHI, Kisaku TANAKA, Yukio MATSUKI, Yos ...
1983 Volume 47 Issue 11 Pages
2427-2433
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
A rapid and specific method is described for the determination of nitrate in meat and fishery products.
Nitrate separated from foods by extraction with 1/50N sodium hydroxide and ultra filtration was readily reduced to nitrite by the use of respiratory nitrate reductase (NR) from Escherichia coli K-12. The nitrite so obtained can be determined by the specific diazotation-coupling reaction method.
The use of an enzymatic reaction resulted in quantitative reduction of nitrate, and the method was relatively free of interferences. Recoveries of 10 and 100 ppm of nitrate from 5 samples of meat and fishery products ranged from 92.8 to 97.8% for 10 ppm and 97.8 to 99.4% for 100 ppm with a detection limit of 0.5 ppm.
View full abstract
-
Yuji HOSHI, Fumio YAMAUCHI
1983 Volume 47 Issue 11 Pages
2435-2440
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Sulfhydryl (SH) and disulfide (SS) contents of soybean 11S globulin (var. Raiden) were determined by means of Ellman's reagent. The amounts of surface SH, internal SH, and SS bonds of 11S globulin (not lyophilized) were 10.3, 4.6, and 17 mol/mol protein, respectively. On the other hand, when the 11S globulin was lyophilized, the surface and internal SH diminished to 5 and 3.6 mol/mol protein, respectively, and the SS bonds increased to 20.1 mol/mol protein. The result from sodium dodecyl sulfate polyacrylamide gel electrophoresis suggested the possibility that the newly formed SS bonds probably existed in each constituent subunit of 11S globulin and/or between the intermediary subunits which exist by nature. Differences and similarities between our result and those obtained by various workers were also discussed.
View full abstract
-
Kimiko OHTANI, Akira MISAKI
1983 Volume 47 Issue 11 Pages
2441-2451
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
β-D-Galactosidase was purified 115-fold from a saline extract of papaya seeds by fractionation with ammonium sulfate, DEAE-Sephadex chromatography and gel-filtration on Sephadex G-75, G-150, and G-100. The purified β-D-galactosidase (MW, 56, 000 daltons) had an isoelectric point (pI) at pH 8.4 and the optimal pH for its activity was 3.5 to 4.5. The enzyme activity was inhibited by Cu
2+, Ag
+, Hg
2+, Pb
2+, NaAsO
2 and
p-chloromercuribenzoate at concentrations of 1×10
-3M. Among the various mono- and oligosaccharides tested, D-galactose, D-galacturonic acid, D-galactono-γ-lactone and melibiose significantly inhibited the enzyme activities at concentrations of 2×10
-3 to 1×10
-2M. The purified enzyme hydrolyzed
p-nitrophenyl β-D-galactoside (
Km= 1.0×10
-3M), methyl β-D-galactoside (
Km=1.6×10
-2M), aminoethyl β-D-galactoside (
Km= 3.3×10
-2M) and lactose (
Km=9.1×10
-2M). β-(1→3)-Linked galactotetraosyl-erythritol and asialo-glycopeptide isolated from fetuin were also hydrolyzed to the extent of 78 and 75%, respectively, on the basis of their galactose contents.
α-D-Mannosidase from papaya seeds was also purified 130-fold by ammonium sulfate fractionation, DEAE-Sephadex chromatography, gel-filtration on Sephadex G-150 and hydroxylapatite chromatography. The purified enzyme (MW, 156, 000 daltons), consisting of two subunits (78, 000×2), was inhibited by Hg
2+, Ag
+, Cu
2+,
p-chloromercuribenzoate, D-glucose, D-glucosamine and D-mannose at concentrations of 1×10
-3 to 1×10
-2M. The α-D-mannosidase hydrolyzed
p-nitrophenyl α-D-mannoside (Km=5.6×10
-3M), methyl α-D-mannoside (Km= 2.8×10
-2M), α-D-mannosyl-D-mannitol (Km=2.2×10
-2M), α-(1→2)-linked D-mannobiosyl-D-mannitol (Km=6.3×10
-3M) and D-mannotriosyl-D-mannitol (Km=5.3×10
-3M).
View full abstract
-
Van Thanh Vo, Isao KUSAKABE, Kazuo MURAKAMI
1983 Volume 47 Issue 11 Pages
2453-2459
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Two fish aminopeptidases designated as aminopeptidases I and II were purified by DEAE-cellulose chromatography, gel filtration on Sephadex G-200, and isoelectric focusing. The final preparations of enzymes I and II were judged nearly homogenous by polyacrylamide gel electrophoresis. The molecular weights of enzymes I and II were determined by gel filtration to be 370, 000 and 320, 000, respectively. The isoelectric points were 4. 1 (I) and 4.8 (II). Both enzymes were inhibited by EDTA and activated by Co
++. Bestatin could inhibit enzyme I but not enzyme II. Enzymes I and II rapidly hydrolyzed not only synthetic substrates containing alanine or leucine but also di-, tri-, and tetra-alanine. Judged from all of these properties, sardine aminopeptidases resemble human alanine aminopeptidase. Enzyme I retained more than 70% of its original activity in 15% NaCl, suggesting the enzyme participates in hydrolyzing fish proteins and peptides during fish sauce production.
View full abstract
-
Tsutomu YAMAGUCHI, Keiko NAKAGAWA
1983 Volume 47 Issue 11 Pages
2461-2465
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Dihydroxyacetone, glyceraldehyde, glyoxal, methyl glyoxal, and glyoxylic acid were found to show mutagenicity on
Salmonella typhimurium TA 100. The mutagenicities of these substances were inhibited by the addition of S-9 or some free radical scavengers. The alkaline buffered solutions of these mutagenic substances were found to reduce Nitro Blue tetrazolium chloride. DNA was degraded by the addition of these mutagenic substances. It has also been confirmed that free radicals derived from autoxidation of these substances are responsible for their mutagenicity.
View full abstract
-
Masaru IIZUKA, Yasuhiko TORII, Nobutaka FUJISAWA, Senji SAKANAKA, Take ...
1983 Volume 47 Issue 11 Pages
2467-2473
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
1. The liberation of invertase (β-fructofuranosidase, EC3.2.1.26) from
Candida utilis at autolysis of the cells was found to begin after the autolysis was almost completed. The autolysis residue at this stage consisted mainly of cell walls (ghosts). A suspension of washed cell ghosts released invertase on further incubation and this liberation was stimulated by the addition of reducing agents such as mercaptoethanol, or proteolytic enzymes such as papain, as has been known in the release of the invertase of
Saccharomyces cerevisiae.
2. The invertase activity of the cell ghosts was not lost when the suspension was heated at 60°C. However, the invertase of the heated cell ghosts was not liberated even if the above stimulative agents were added.
3. Several commercial enzymes were shown to stimulate the liberation of invertase from the heated cell ghosts and "Zymolyase, " one of the effective enzymes, was fractionated. One fraction isolated from the preparation showed a striking effect on the liberation of invertase but this fraction did not show lytic activity on brewer's yeast cells.
View full abstract
-
Tatsunori YAMAGISHI, Tomonari TOMISAWA, Fumio YAMAUCHI
1983 Volume 47 Issue 11 Pages
2475-2481
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Heating 11S globulin in the presence of
N-ethylmaleimide (NEM) gave buffer-soluble aggregates and dissociates. The difference-second derivative absorption spectra indicated that the aggregates had larger internal hydrophobicity than 11S globulin, while that of the dissociates was conversely smaller. The protein's fluorescence spectra indicated that, compared with 11S globulin, the wavelength of the fluorescence peak of the aggregates was hardly shifted, while that of the dissociates was red-shifted. The circular dichroism of the aggregates was similar to that of 11S globulin.
These results suggest that the aggregates were formed with retention of the internal hydrophobic region of 11S globulin, while the dissociates released from 11S globulin were unfolded with increasing heating time.
View full abstract
-
Akira IWAYAMA, Tomio KIMURA, Osao ADACHI, Minoru AMEYAMA
1983 Volume 47 Issue 11 Pages
2483-2493
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
A new N-terminal exopeptidase, L-tryptophan aminopeptidase, was purified and crystallized from the cell-free extract of
Trichosporon cutaneum. Enzyme purification was performed by a method involving heat treatment, ammonium sulfate fractionation, chromatographies on DEAE-cellulose and hydroxyapatite columns, and isoelectrofocusing. The enzyme was purified about 1, 600-fold with an overall yield of 23%. The crystallized enzyme was homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was determined to be 270, 000 by gel filtration and the enzyme was dissociated into four subunits having a molecular weight of 68, 000 upon sodium dodecylsulfate polyacrylamide gel electrophoresis. L-Tryptophanamide and dipeptides possessing L-tryptophan at the N-terminal moiety were the most favorable substrates. The enzyme activity was absolutely dependent on Mn
2+. The enzyme catalyzed the hydrolysis at pH9.0 to 9.5 most rapidly. Other catalytic and physicochemical properties of the enzyme were also examined in some detail.
View full abstract
-
Tomoyuki TSUNEYA, Masakazu ISHIHARA, Haruyasu SHIOTA, Minoru SHIGA
1983 Volume 47 Issue 11 Pages
2495-2502
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Steam distilled oil of quince fruit (
Cydonia oblonga Mill.=
C. vulgaris Pers., marmelo in Japanese) was analyzed by gas chromatography and gas chromatography-mass spectrometry. Sixty-two compounds, 2 hydrocarbons, 13 esters, 11 alcohols, 11 aldehydes, 11 ketones, 5 lactones and 9 miscellaneous compounds, were identified. Of them, the chemical structures of two new oxidecompounds,
trans- and
cis-3-methyl-5-[(
E)-3'-methyl-1', 3 '-butadien-1'-yl]tetrahydrofuran, were elucidated by instrumental analyses.
View full abstract
-
Mikio KAWAMORI, Yukio HASHIMOTO, Ryoichi KATSUMATA, Ryo OKACHI, Kenich ...
1983 Volume 47 Issue 11 Pages
2503-2509
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
A search was undertaken for microorganisms that can catalyze the enzymatic production of amoxicillin.
Pseudomonas melanogenum KY 3987 was selected from our stock cultures, β-Lactamase-deficient mutants were isolated from amoxicillin-sensitive mutants derived from this strain. These mutants became sensitive to other penicillins and cephalosporins as well as amoxicillin and did not produce β-lactamase even in the presence of an inducer, such as penicillin V. Amoxicillin was effectively synthesized from D-2-
p-hydroxyphenylglycine methyl ester and 6-aminopenicillanic acid (6-APA) with these mutants as the enzyme sources. The conversion ratio from 6-APA to amoxicillin was about 90% as a mol ratio.
View full abstract
-
Nobuya ITOH, Ryoko MORIKAWA
1983 Volume 47 Issue 11 Pages
2511-2519
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
L-Alanine dehydrogenase was found to be widely distributed in
Streptomyces species, and high enzyme activity was observed in
Streptomyces phaeochromogenes. The enzyme was purified to homogeneity from a cell-free extract of
S. phaeochromogenes IFO 3149 by precipitation with ammonium sulfate and column chromatography on DEAE-cellulose, Blue-Sepharose CL-4B and Sephadex G-200, and then crystallized. The enzyme had a molecular weight of 240, 000, and was composed of six identical subunits. The enzyme almost specifically catalyzed the oxidative deamination of L-alanine. In the reductive aminating reaction, the enzyme acted on several 2-oxo acids. The enzyme required NAD
+ as a co factor, and showed only slight activity with NADP
+. The enzyme showed maximum activity at pH 10.0 in the deaminating reaction and at pH 8.0 in the aminating reaction.
View full abstract
-
Katsuhisa HONDA, Muhammad SAHRUL, Hideo HIDAKA, Ryo TATSUKAWA
1983 Volume 47 Issue 11 Pages
2521-2532
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Bioaccumulation of heavy metals in Antarctic fish remains to be studied. This paper reports the concentrations and distribution of heavy metals in organs and tissues of Antarctic fish,
Pagothenia borchgrevinki, collected around the Syowa Station, Antarctica, during 1981, and also discusses the growth-related changes of heavy metal accumulation.
The metal concentrations of the whole fish were lower for iron and mercury, and higher for cadmium compared with those of fishes from other oceans. Generally, high concentrations of the metals were observed in the liver, and low ones in the muscle. However, the concentrations of manganese, zinc, copper, lead and nickel were relatively high in the ovary and testis also, and those of manganese and zinc were the highest in the skin. Relatively high concentrations of cadmium and mercury were also found in the testis. Approximately 60% of the metal burden in the whole fish was on their muscle and bone which comprised an average of 80% of the body weight. However, a relatively high burden of iron, cadmium and mercury, in particular a high burden of cadmium, say about 40%, was found in the liver.
The concentration of metals in the organs and tissues characteristically changed with the growth of the fish. The small fish showed faster uptake and excretion rates of metals than the large ones. The accumulation of cadmium and mercury in fish depended on the exposure time. In contrast, for the accumulation of iron, manganese, zinc and copper, the metabolic turnover was a dominant factor, and that for lead and nickel is also likely to be so. These results indicate that consideration of the growth stage of the organ and tissue is needed for detailed understanding of the bioaccumulation process and also for toxicological criteria of heavy metals.
View full abstract
-
Shigeyuki TAKENISHI, Yasuto WATANABE, Tan Miwa, Reisuke KOBAYASHI
1983 Volume 47 Issue 11 Pages
2533-2540
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
β-Galactosidase of a strain of
Penicillium multicolor was purified to homogeneity from culture broth. The enzyme was most active at pH 4.0 and at 60°C, and was stable in the pH range 3.5 to 7.5 and below 45°C. Only β-D-galactosides could be substrates. The activity to ONPG was highest among the galactosides tested and about 2-times higher than that to lactose. The apparent
Km values were 0.6 and 8.9mM for ONPG and lactose, respectively. Hg
2+ and Cu
2+ inhibited the activity while the other metal ions tested had no effect. p-Aminophenyl β-D-thiogalactopyranoside inhibited the activity competitively. The molecular weight of the enzyme was estimated to be 1.26×10
5 and 1.3×10
5 by sedimentation equilibrium and SDS-polyacrylamide gel electrophoresis, respectively. Leucine and glycine were the N- and C-terminal residues, respectively.
View full abstract
-
Ryoichi SAKATA, Kenichi SHUTO, Yukiharu NAGATA
1983 Volume 47 Issue 11 Pages
2541-2546
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
To clarify the reason for the decrease in CFR (color forming ratio) of pale, soft and exudative (PSE) porcine muscle, the effect of simulation of the PSE conditions on cooked cured meat color was investigated in fractionated components from porcine skeletal muscle, 24hr postmortem. Although the solubility of total proteins and heme pigments markedly decreased in sarcoplasm by this treatment, no decline in CFR of the sarcoplasm could be observed when compared to the controls. A similar tendency was observed in both high- and low-molecular weight fractions of sarcoplasm. On the other hand, myofibrils simulated the PSE conditions in the presence of myoglobin significantly decreased CFR, and the extent of this decline was nearly consistent with the case of whole muscle. The reasons for the decrease in CFR of PSE muscle are discussed.
View full abstract
-
J. J. ALLAIS, A. LOUKTIBI, J. BARATTI
1983 Volume 47 Issue 11 Pages
2547-2554
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The formate dehydrogenase from the yeast
Pichia pastoris IFP 206 was purified to homogeneity. The protein showed a molecular weight of 68, 000 daltons and was composed of two identical subunits. Its amino acid composition was similar to those of other formate dehydrogenases and was characterized by a high content of acidic residues. The N-terminal end of the molecule was probably blocked.
The enzyme activity was NAD
+ dependent (NADP
+ could not replace NAD
+). Its optimum temperature was 47°C and the activation energy 10.8 kcal/mol. The enzyme was active from pH 3.5 to 10.5 with a maximum at pH 7.5. The Michaelis constant for NAD
+ and formate were respectively 0.27 and 15 mM. The purified enzyme had no S-formylgmtathione hydrolase activity, strongly suggesting that the true substrate was formate. NADH, cyanide and azide were strong inhibitors of the enzyme.
View full abstract
-
Kimikazu IWAMI, Akio NAKAMURA, Masako HIGUCHI, Kyoden YASUMOTO, Kazuo ...
1983 Volume 47 Issue 11 Pages
2555-2559
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The bioavailability of L-methionine sulfoxide was evaluated by measuring the restoration of the liver glutathione level following amino acid administration, the sulfur incorporation into liver glutathione molecules, and the urinary excretion of inorganic sulfate. The amino acid was administered by intraperitoneal injection (at a level of 150μmol/animal once a day) to rats fed a 10% casein diet for 3 weeks. Two or three injections of the amino acid led to a partial restoration of the decreased glutathione level in the liver. The magnitude of the increase was below the expectation from equivalent methionine administration. Similar effects were substantiated by experiments with [
35S]-labeled amino acids, in which the sulfur of L-methionine sulfoxide was incorporated into the glutathione molecule with half the effectiveness of L-methionine. Inorganic sulfate predominated in the sulfur metabolites in the urine of rats given [
35S] methionine, while sulfate excretion accounted for only a half of the sulfur metabolites in the urine of rats given [
35S] methionine sulfoxide. Provided that methionine sulfoxide is converted to methionine prior to its incorporation into liver glutathione as well as its excretion as inorganic sulfate in the urine, the glutathione and sulfate measurements can be taken as reliable indices to evaluation of methionine sulfoxide bioavailability.
View full abstract
-
Bong-Sun PARK, Aiko HIROTANI, Yoshihisa NAKANO, Shozaburo KITAOKA
1983 Volume 47 Issue 11 Pages
2561-2567
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
While arginine was not taken up by
Euglena gracilis and accordingly did not support the growth of this protozoan, it was accumulated in both free and peptide forms as a major nitrogen reserve in the cells, when a relative excess of a nitrogen source was supplied. Its content was greatest in the early exponential phase of growth, reaching as high a concentration as 220μmol per 10
9 cells or 190mM in the cell volume. In the mid-exponential phase it decreased and accumulated again in the late-exponential phase. Addition of ethanol or glucose to a culture of
E. gracilis in the late-exponential phase rapidly eliminated the accumulated arginine with renewed cell division, and the further addition of ammonium salts or the amino acids caused renewed accumulation of arginine. The degradation of accumulated arginine involved
de novo synthesis of enzymes related to arginine metabolism. Analysis of metabolic products after incubation of labelled arginine in cell-free extracts and assay of related enzymes showed that in
Euglena arginine is catabolized to ornithine via citrulline by the so-called arginine dihydrolase pathway, releasing ammonia successively. The enzymes involved in this pathway, arginine deiminase and citrullinase, had different optimum pH values from those of other organisms.
View full abstract
-
Kenji AOKI, Kotaro OHTSUKA, Ryu SHINKE, Hiroshi NISHIRA
1983 Volume 47 Issue 11 Pages
2569-2575
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Twenty bacterial strains were isolated from soil, when aniline was provided as a sole source of carbon and nitrogen.
Rhodococcus erythropolis AN-13, one of the isolates, grew on aniline at concentrations from 0.65 to 2.6 mg/ml and completely degraded it. Ammonia was released from aniline with cell growth and accumulated in the cultural broth. Aniline-grown cells of this bacterium oxidized aniline and catechol, but did not take up a significant amount of oxygen in the presence of o- or p-aminophenol. These facts suggest that
R. erythropolis AN-13 metabolized aniline through catechol. Additional carbon and nitrogen sources did not cause any repression of aniline biodegradation in this strain, but promoted its breakdown with an increase of cell growth. The bacterium used aniline in preference to glucose in a medium containing these two substrates.
View full abstract
-
Kimio NISHIMURA, Yukio KAWAMURA, Teruyoshi MATOBA, Daizo YONEZAWA
1983 Volume 47 Issue 11 Pages
2577-2583
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The species of endogenous proteases in Antarctic krill,
Euphausia superba, were investigated using the homogenate of krill and the active fractions after gel filtration of the homogenate as to the following criteria : Substrate specificity (benzyloxycarbonyl (Z)-Phe-Ala, Z-Glu-Tyr, hippuryl-Arg, hippuryl-Phe, benzoyl Arg-p-nitroanilide, Leu-p-nitroanilide,
14C-hemoglobin), sensitivity to protease inhibitors (diisopropyl fluorophosphate, iodoacetamide, EDTA, soybean trypsin inhibitor and pepstatin), molecular weight and isoelectric point.
From the experimental results, we found that the carboxypeptidase A and B, aminopeptidase, trypsin and cathepsin A types of proteases were present in krill.
View full abstract
-
Mikihiko KOBAYASHI, Shiro TAKAGI, Masao SHIOTA, Yasushi MITSUISHI, Kaz ...
1983 Volume 47 Issue 11 Pages
2585-2593
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
An isomaltotriose-producing dextranase II, detected in the culture supernatant of
Flavobacterium sp. M-73, was purified to an electrophoretically pure state. Successive chromatography on hydrophobic columns of Amberlite CG-50 and aminooctyl-Sepharose was very effective as the first step of purification. Further purification of the enzyme was performed by affinity column chromatography on isomaltotriose-Sepharose and preparative polyacrylamide gel electrophoresis.
The purified enzyme was shown to be a monomer and had a molecular weight of 114, 000. Dextranase II was most active at pH 7.0 and 35°C. It was stable at 4°C for 24hr over a pH range of 6.5-12.0 and up to 35°C on heating for 10 min. This enzyme had a strict specificity for consecutive α-1, 6-glucosidic linkages and readily hydrolyzed clinical dextran and Sephadex gels. The degree of hydrolysis of clinical dextran was 31% expressed as apparent conversion into D-glucose. The amount of isomaltotriose in the hydrolyzate was determined to be 63%.
View full abstract
-
Shuji SENDA, Kenji MORI
1983 Volume 47 Issue 11 Pages
2595-2598
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Optically pure (R, Z)-(-)-5-(1-deceny1)oxacyclopentan-2-one, the pheromone of
Popillia japonica, was synthesized by employing the asymmetric reduction of an acetylenic keto ester as the key-step.
View full abstract
-
Shigefumi KUWAHARA, Kenji MORI
1983 Volume 47 Issue 11 Pages
2599-2606
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The three possible stereoisomers of 13, 23-dimethylpentatriacontane, a tsetse fly pheromone, were synthesized starting from optically pure (R)-(+)-citronellic acid. (13R, 17R)-13, 17-Dimethylpentatriacontane was also synthesized.
View full abstract
-
Yoshiyuki KURATSU, Yuko ARAI, Keiichi INUZUKA, Takeo SUZUKI
1983 Volume 47 Issue 11 Pages
2607-2612
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
The effect of amino acids on colistin production was investigated with
Bacillus polymyxa var. KY-7584. Aspartic acid, the precursor of α, γ-diaminobutyric acid (one of the structural components of colistin), showed a remarkable difference of colistin production between Morido's fermentation medium and the modified medium containing the appropriate concentrations of phosphate ion (PO
43-) and ammonium-nitrogen (NH
4-N). Further studies revealed that a main factor which controlled the stimulatory effect of aspartic acid on colistin production was PO
43-.The optimum concentrations of aspartic acid, PO
43- and NH
4-N in the medium for colistin production were above 0.2%, below 0.01% and 0.17%, respectively. The maximum titer of colistin (51, 900u/ml) by the addition of 0.25% aspartic acid showed the increment of about 30% as compared with that in the reference medium. However, the increase of cell concentration was slight.This study also showed that PO
43- was an effector to inhibit the metabolic pathway from aspartic acid to α, γ-diaminobutyric acid.
View full abstract
-
Takayuki ORITANI, Michio ICHIMURA, Yoshifumi HANYU, Kyohei YAMASHITA
1983 Volume 47 Issue 11 Pages
2613-2617
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Asymmetric hydrolysis of chloroacetates of (±)-
axial-alcohols (±)-neomenthol
(2), (1RS, 4aRS, 8aSR)-decahydro-1-naphthol (
6) by
Trichoderma koningi gave (-)-(1S, 3R, 4R)-neomenthol (
2) (54% optical purity, o.p.) and (-)-(1R, 4aR, 8aS)-decahydro-1-naphthol (
6) (66% o.p.) with their enantiomeric chloroacetates. However, the chloroacetate of (2RS, 4aRS, 8aSR)-decahydro-2-naphthol (
10) was hydrolyzed by
T. koningi to give the (-)-alcohol (
10) (12% o.p.) with low enantioselectivity.
View full abstract
-
Masako OOGAKI, Tadaatsu NAKAHARA, Hiroo UCHIYAMA, Takeshi TABUCHI
1983 Volume 47 Issue 11 Pages
2619-2624
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Under thiamine-deficient, aerobic culture conditions,
Yarrowia lipolytica was found to produce D-(+)-2-hydroxyglutaric acid extracellularly in amounts of about 5mg per ml of the culture filtrate, together with pyruvic and 2-ketoglutaric acids, from glucose or glycerol in a chemically defined medium. Under similar conditions, however, only a small amount of the hydroxy acid was produced from odd- or even-numbered n-alkanes.
View full abstract
-
Ryo YAMAUCHI, Masahiro KOJIMA, Koji KATO, Yoshimitsu UENO
1983 Volume 47 Issue 11 Pages
2625-2630
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
Neat monogalactosyldilinolenoylglycerol (di-18:3 MGDG) and digalactosyldilinolenoylglycerol (di-18:3 DGDG) were autoxidized at 37°C. The rate of autoxidation of di-18:3 MGDG was greater than that of di-18:3 DGDG. The oxidation products were separated from unoxidized di-18:3 MGDG and di-18:3 DGDG by reverse-phase high performance liquid chromatography (HPLC). The products separated by HPLC were shown to be made up of lipid peroxides formed by free radical oxidation of the linolenate component of the MGDG and DGDG. Each linolenoyl moiety in the MGDG and DGDG produced isomeric peroxides in a manner similar to methyl linolenate.
View full abstract
-
Toshiro KOZONO, Tatsuhiko KANMERA, Tetsuo KATO, Tamio UENO, Nobuo IZUM ...
1983 Volume 47 Issue 11 Pages
2631-2632
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Tomiko ISOHATA, Keiko ABE, Seiichi HOMMA, Masao FUJIMAKI, Soichi ARAI
1983 Volume 47 Issue 11 Pages
2633-2635
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Shinji KAMATA, Heiichi SAKAI, Akira HIROTA
1983 Volume 47 Issue 11 Pages
2637-2638
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Kohji TADASA, Hiroshi KAYAHARA
1983 Volume 47 Issue 11 Pages
2639-2640
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Tsutomu YOSHIDA, Shoko SHINODA, Michiko NAGATA
1983 Volume 47 Issue 11 Pages
2641-2644
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Kiyoshi HAYASHI, Takafumi KASUMI, Naoya KUBO, Nobuzo TSUMURA
1983 Volume 47 Issue 11 Pages
2645-2646
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Takanori KASAI, Tsuyoshi NISHITOBA, Sadao SAKAMURA
1983 Volume 47 Issue 11 Pages
2647-2649
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Hikaru SUENAGA, Seiya OGATA, Shinsaku HAYASHIDA
1983 Volume 47 Issue 11 Pages
2651-2652
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Masatoshi HAYASHI, Kojiro WADA, Katsura MUNAKATA
1983 Volume 47 Issue 11 Pages
2653-2655
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
K. VASU, N. K. ROY
1983 Volume 47 Issue 11 Pages
2657-2659
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Nobuko MINAGAWA, Akio YOSHIMOTO
1983 Volume 47 Issue 11 Pages
2661-2663
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Yil KIM, Rikimaru HAYASHI
1983 Volume 47 Issue 11 Pages
2665-2667
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Hiroshi INUI, Kazutaka MIYATAKE, Yoshihisa NAKANO, Shozaburo KITAOKA
1983 Volume 47 Issue 11 Pages
2669-2671
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Kanzo SAKATA, Toshiaki KUWATSUKA, Akira SAKURAI, Nobutaka TAKAHASHI, G ...
1983 Volume 47 Issue 11 Pages
2673-2674
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Takashi OKAMOTO, Yasuhito FUJITA, Ryozaburo IRIE
1983 Volume 47 Issue 11 Pages
2675-2676
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Toshiaki UMEZAWA, Fumiaki NAKATSUBO, Takayoshi HIGUCHI
1983 Volume 47 Issue 11 Pages
2677-2681
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Yoshihiro NISHIDA, Toshio KONNO, Hiroshi OHRUI, Hiroshi MEGURO
1983 Volume 47 Issue 11 Pages
2683-2684
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Chol CHO, Yukihiro SUGIMOTO, Jin-Myeon KIM, Hideaki USUDA, Ryuichi ISH ...
1983 Volume 47 Issue 11 Pages
2685-2687
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Ichiro YAMASHITA, Sakuzo FUKUI
1983 Volume 47 Issue 11 Pages
2689-2692
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Yoji MIKAMI, Toshiyuki SUZUKI
1983 Volume 47 Issue 11 Pages
2693-2695
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Hiroyuki NISHIMURA, Shigeru HIRAMOTO, Junya MIZUTANI, Yoshiaki NOMA, A ...
1983 Volume 47 Issue 11 Pages
2697-2699
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Yoshiki KONO, Setsuo TAKEUCHI, J. M. DALY
1983 Volume 47 Issue 11 Pages
2701-2702
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS
-
Yuichi ABE, Jun-ichi KADOKURA, Akira SHIMAZU, Haruo SETO, Noboru OTAKE
1983 Volume 47 Issue 11 Pages
2703-2705
Published: 1983
Released on J-STAGE: March 27, 2006
JOURNAL
FREE ACCESS